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TitleEvidence for a Boat Conformation at the Transition State of Gh76 Alpha-1,6-Mannanases- Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 54, Page 5378-, Year 2015
Publish dateOct 27, 2014 (structure data deposition date)
AuthorsThompson, A.J. / Speciale, G. / Iglesias-Fernandez, J. / Hakki, Z. / Belz, T. / Cartmell, A. / Spears, R.J. / Chandler, E. / Temple, M.J. / Stepper, J. ...Thompson, A.J. / Speciale, G. / Iglesias-Fernandez, J. / Hakki, Z. / Belz, T. / Cartmell, A. / Spears, R.J. / Chandler, E. / Temple, M.J. / Stepper, J. / Gilbert, H.J. / Rovira, C. / Williams, S.J. / Davies, G.J.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:25772148
MethodsX-ray diffraction
Resolution1.2 - 1.4 Å
Structure data

PDB-4d4a:
Structure of the catalytic domain (BcGH76) of the Bacillus circulans GH76 alpha mannanase, Aman6.
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-4d4b:
The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with MSMSMe
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-4d4c:
The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with 1,6-ManDMJ
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-4d4d:
The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with 1,6-ManIFG
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-5agd:
An inactive (D125N) variant of the catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with alpha-1,6-mannopentaose
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-DMJ:
1-DEOXYMANNOJIRIMYCIN

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-IFM:
5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE

Source
  • bacillus circulans (bacteria)
KeywordsHYDROLASE / GLYCOSIDE HYDROLASE / GH76 / CAZY / MANNAN / ENZYME-CARBOHYDRATE INTERACTION / GLYCOSIDASE INHIBITION / QUANTUM MECHANICS / TRANSITION STATE / ALPHA-MANNANASE / MANNANASE

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